CAZyme Information: MGYG000003016_02395

Basic Information

• Species: Salinicola tamaricis
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Halomonadaceae; Salinicola; Salinicola tamaricis
• CAZyme ID: MGYG000003016_02395
• CAZy Family: GH43
• CAZyme Description: Xylan 1,3-beta-xylosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
322		36576.07	5.7248

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003016	3944563	MAG	China	Asia

• Gene Location: Start: 63; End: 1031 Strand: +

Full Sequence      

MARSRELTGPYEVDPTNPVLTSNPNARDQLQKAGHGSLVETPGGEWYCAHLCARPVVAGR
CILGRETALQRCVWTEDDWLRIDGGPYPSHRVAGPHLAWQPPPAEPDRDTFERPSLHRYW
QSLRRPFDDTWLSLSERPGCLRLKGGESMQSTHRQSLLARRLSHFELEVETRLSFDPEHF
QQMAGLILYYDAKDYVYLRVTREETLGRCLGIVVSRHGVYDEPLTADVPLMAGDVRLMAR
LAREKLRFFHAPVDTQGDPDRHADAVDWQPIGDPLDISHLCDDDPDYIRFTGTFVGLCAQ
DLSGAGLAADFHEFDYRPEKSR

Enzyme Prediction     

EC	3.2.1.37

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3507	XynB2	8.57e-89	1	318	236	548	Beta-xylosidase [Carbohydrate transport and metabolism].
pfam17851	GH43_C2	3.02e-64	108	317	1	203	Beta xylosidase C-terminal Concanavalin A-like domain. This domain is found to the C-terminus of the pfam04616 domain. This domain adopts a concanavalin A-like fold.
cd09000	GH43_SXA-like	1.10e-42	1	82	210	292	Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA. This glycosyl hydrolase family 43 (GH43) includes enzymes that have been characterized to mainly have beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium (Xsa;Sxa;SXA), Bifidobacterium adolescentis ATCC 15703 (XylC;XynB;BAD_0428) and Bacillus sp. KK-1 XylB. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. These enzymes possess an additional C-terminal beta-sandwich domain that restricts access for substrates to a portion of the active site to form a pocket. The active-site pockets comprise of two subsites, with binding capacity for two monosaccharide moieties and a single route of access for small molecules such as substrate. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
pfam04616	Glyco_hydro_43	9.62e-24	1	79	204	280	Glycosyl hydrolases family 43. The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyze the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd08989	GH43_XYL-like	3.14e-23	2	75	200	272	Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium beta-D-xylosidase SXA. These are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. It also includes various GH43 family GH43 arabinofuranosidases (EC 3.2.1.55) including Humicola insolens alpha-L-arabinofuranosidase AXHd3, Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB), and the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl). GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABE58499.1	3.97e-137	1	318	215	521
QEL10031.1	6.08e-135	1	321	215	524
ASS92940.1	7.78e-130	1	317	215	520
QJX61583.1	5.58e-129	1	316	215	519
QKH60752.1	3.18e-128	1	316	215	519

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1YRZ_A	9.02e-103	1	317	216	524	ChainA, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125],1YRZ_B Chain B, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125]
6IFE_A	3.57e-60	1	316	232	548	AGlycoside Hydrolase Family 43 beta-Xylosidase [Bacillus pumilus],6IFE_B A Glycoside Hydrolase Family 43 beta-Xylosidase [Bacillus pumilus]
7K1R_A	1.45e-58	3	318	216	535	ChainA, Beta xylosidase GH43 [Enterobacter sp. enrichment culture clone nf1B6],7K1R_B Chain B, Beta xylosidase GH43 [Enterobacter sp. enrichment culture clone nf1B6],7K1R_C Chain C, Beta xylosidase GH43 [Enterobacter sp. enrichment culture clone nf1B6],7K1R_D Chain D, Beta xylosidase GH43 [Enterobacter sp. enrichment culture clone nf1B6]
1YIF_A	7.35e-58	1	317	214	531	CRYSTALSTRUCTURE OF beta-1,4-xylosidase FROM BACILLUS SUBTILIS, NEW YORK STRUCTURAL GENOMICS CONSORTIUM [Bacillus subtilis],1YIF_B CRYSTAL STRUCTURE OF beta-1,4-xylosidase FROM BACILLUS SUBTILIS, NEW YORK STRUCTURAL GENOMICS CONSORTIUM [Bacillus subtilis],1YIF_C CRYSTAL STRUCTURE OF beta-1,4-xylosidase FROM BACILLUS SUBTILIS, NEW YORK STRUCTURAL GENOMICS CONSORTIUM [Bacillus subtilis],1YIF_D CRYSTAL STRUCTURE OF beta-1,4-xylosidase FROM BACILLUS SUBTILIS, NEW YORK STRUCTURAL GENOMICS CONSORTIUM [Bacillus subtilis]
5ZQJ_A	1.20e-57	1	316	214	530	Crystalstructure of beta-xylosidase from Bacillus pumilus [Bacillus pumilus],5ZQJ_B Crystal structure of beta-xylosidase from Bacillus pumilus [Bacillus pumilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A9ZND1	9.78e-60	1	316	217	532	Xylan 1,3-beta-xylosidase OS=Vibrio sp. OX=678 GN=xloA PE=1 SV=1
P77713	5.38e-59	3	318	216	535	Putative beta-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yagH PE=3 SV=1
P94489	1.05e-57	1	317	214	531	Beta-xylosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=xynB PE=1 SV=2
P07129	5.86e-57	1	316	214	530	Beta-xylosidase OS=Bacillus pumilus OX=1408 GN=xynB PE=1 SV=2
A7LXU0	2.02e-24	3	317	228	526	Non-reducing end alpha-L-arabinofuranosidase BoGH43B OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02656 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000049	0.000010	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003016_02395.